ID   YB51_ENCCU              Reviewed;         254 AA.
AC   Q8SU65;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Polysaccharide deacetylase domain-containing protein ECU11_0510;
GN   OrderedLocusNames=ECU11_0510;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], DEVELOPMENTAL
RP   STAGE, AND SUBCELLULAR LOCATION.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX   PubMed=19472335; DOI=10.1002/pro.128;
RA   Urch J.E., Hurtado-Guerrero R., Brosson D., Liu Z., Eijsink V.G.,
RA   Texier C., van Aalten D.M.;
RT   "Structural and functional characterization of a putative polysaccharide
RT   deacetylase of the human parasite Encephalitozoon cuniculi.";
RL   Protein Sci. 18:1197-1209(2009).
CC   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
CC   -!- CAUTION: Although it contains a polysaccharide deacetylase domain, the
CC       protein does not display any chitin deacetylase activity.
CC       {ECO:0000305|PubMed:19472335}.
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DR   EMBL; AL590450; CAD25961.1; -; Genomic_DNA.
DR   RefSeq; NP_586357.1; NM_001042190.1.
DR   PDB; 2VYO; X-ray; 1.50 A; A=1-254.
DR   PDBsum; 2VYO; -.
DR   AlphaFoldDB; Q8SU65; -.
DR   SMR; Q8SU65; -.
DR   STRING; 284813.Q8SU65; -.
DR   GeneID; 860010; -.
DR   KEGG; ecu:ECU11_0510; -.
DR   VEuPathDB; MicrosporidiaDB:ECU11_0510; -.
DR   HOGENOM; CLU_1082481_0_0_1; -.
DR   InParanoid; Q8SU65; -.
DR   OrthoDB; 1132954at2759; -.
DR   EvolutionaryTrace; Q8SU65; -.
DR   Proteomes; UP000000819; Chromosome XI.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; SSF88713; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome.
FT   CHAIN           1..254
FT                   /note="Polysaccharide deacetylase domain-containing protein
FT                   ECU11_0510"
FT                   /id="PRO_0000383036"
FT   DOMAIN          26..210
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT   STRAND          23..34
FT                   /evidence="ECO:0007829|PDB:2VYO"
FT   HELIX           40..51
FT                   /evidence="ECO:0007829|PDB:2VYO"
FT   STRAND          56..59
FT                   /evidence="ECO:0007829|PDB:2VYO"
FT   HELIX           67..70
FT                   /evidence="ECO:0007829|PDB:2VYO"
FT   HELIX           71..78
FT                   /evidence="ECO:0007829|PDB:2VYO"
FT   STRAND          82..86
FT                   /evidence="ECO:0007829|PDB:2VYO"
FT   HELIX           89..91
FT                   /evidence="ECO:0007829|PDB:2VYO"
FT   HELIX           95..97
FT                   /evidence="ECO:0007829|PDB:2VYO"
FT   HELIX           100..118
FT                   /evidence="ECO:0007829|PDB:2VYO"
FT   STRAND          124..126
FT                   /evidence="ECO:0007829|PDB:2VYO"
FT   HELIX           136..143
FT                   /evidence="ECO:0007829|PDB:2VYO"
FT   TURN            144..146
FT                   /evidence="ECO:0007829|PDB:2VYO"
FT   HELIX           156..158
FT                   /evidence="ECO:0007829|PDB:2VYO"
FT   STRAND          159..161
FT                   /evidence="ECO:0007829|PDB:2VYO"
FT   HELIX           162..171
FT                   /evidence="ECO:0007829|PDB:2VYO"
FT   TURN            175..177
FT                   /evidence="ECO:0007829|PDB:2VYO"
FT   STRAND          180..185
FT                   /evidence="ECO:0007829|PDB:2VYO"
FT   HELIX           186..189
FT                   /evidence="ECO:0007829|PDB:2VYO"
FT   HELIX           193..205
FT                   /evidence="ECO:0007829|PDB:2VYO"
FT   HELIX           212..215
FT                   /evidence="ECO:0007829|PDB:2VYO"
FT   TURN            216..218
FT                   /evidence="ECO:0007829|PDB:2VYO"
SQ   SEQUENCE   254 AA;  28078 MW;  E351013C3CD40753 CRC64;
     MLLCLLYFTS SWCSGSDVPD VCTNSGMIAI NFVDGPVRGV TDRILNTLDE LGVKATFSFT
     VNQKAVGNVG QLYRRAVEEG HNVALRVDPS MDEGYQCLSQ DALENNVDRE IDTIDGLSGT
     EIRYAAVPIC NGQVNSEMYN ILTERGVLPV GYTFCPYDYD DPVGEFESMI EGSDPKHHSF
     IILMHDGQEA DTSRLENMVK IGKDKGYRFV NMDECLQGYK GAPGDPELSL RGKGVESIGK
     GFLPFFLMML VRLL